id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-000294-2g471tb4	Rhodin, Michael H. J.	A flexible loop in yeast ribosomal protein L11 coordinates P-site tRNA binding	2010-08-12		.txt	text/plain	8139	393	57	High-resolution structures reveal that yeast ribosomal protein L11 and its bacterial/archael homologs called L5 contain a highly conserved, basically charged internal loop that interacts with the peptidyl-transfer RNA (tRNA) T-loop. The two mutants also had opposing effects on binding of aa-tRNA to the ribosomal A-site, and downstream functional effects were observed on translational fidelity, drug resistance/hypersensitivity, virus maintenance and overall cell growth. The high degree of similarity across species, from the primary amino acid sequences to their tertiary structures, suggests conserved functional roles beyond serving as mere scaffolding for the rRNAs. Ribosomal protein L11 of Saccharomyces cerevisiae is an essential, highly conserved component of the 60S subunit (in bacteria and archaea, the homologous protein is named L5; the yeast nomenclature is used throughout this text to minimize confusion). Analysis of the recent cryo-EM yeast ribosome structure (4) revealed that these H84 loop bases are located within 3 Å of the stretches of amino acids changed to alanines in both the 51-4A and 54-7A mutants ( Figure 5B ).	./cache/cord-000294-2g471tb4.txt	./txt/cord-000294-2g471tb4.txt